PEVD1_VERDA
ID PEVD1_VERDA Reviewed; 155 AA.
AC G0Y276; P86840;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Effector protein PevD1 {ECO:0000305};
DE AltName: Full=Hypersensitive response-inducing protein PevD1 {ECO:0000303|PubMed:21691787};
DE Flags: Precursor;
GN Name=PevD1 {ECO:0000303|PubMed:21691787};
OS Verticillium dahliae (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=27337 {ECO:0000312|EMBL:ADW79419.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-88, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21691787; DOI=10.1007/s00253-011-3405-1;
RA Wang B., Yang X., Zeng H., Liu H., Zhou T., Tan B., Yuan J., Guo L.,
RA Qiu D.;
RT "The purification and characterization of a novel hypersensitive-like
RT response-inducing elicitor from Verticillium dahliae that induces
RT resistance responses in tobacco.";
RL Appl. Microbiol. Biotechnol. 93:191-201(2012).
RN [2]
RP FUNCTION, AND DOMAIN.
RX PubMed=24080193; DOI=10.1016/j.micres.2013.08.001;
RA Liu W., Zeng H., Liu Z., Yang X., Guo L., Qiu D.;
RT "Mutational analysis of the Verticillium dahliae protein elicitor PevD1
RT identifies distinctive regions responsible for hypersensitive response and
RT systemic acquired resistance in tobacco.";
RL Microbiol. Res. 169:476-482(2014).
RN [3]
RP FUNCTION.
RX PubMed=24337817; DOI=10.1007/s00299-013-1546-7;
RA Bu B., Qiu D., Zeng H., Guo L., Yuan J., Yang X.;
RT "A fungal protein elicitor PevD1 induces Verticillium wilt resistance in
RT cotton.";
RL Plant Cell Rep. 33:461-470(2014).
RN [4]
RP CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND
RP SUBUNIT.
RX PubMed=22750869; DOI=10.1107/s1744309112020556;
RA Han L., Liu Z., Liu X., Qiu D.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of the effector protein PevD1 from Verticillium dahliae.";
RL Acta Crystallogr. F 68:802-805(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), DISULFIDE BONDS, AND INTERACTION
RP WITH ARABIDOPSIS THALIANA NRP.
RX PubMed=28633330; DOI=10.1093/jxb/erx192;
RA Zhou R., Zhu T., Han L., Liu M., Xu M., Liu Y., Han D., Qiu D., Gong Q.,
RA Liu X.;
RT "The asparagine-rich protein NRP interacts with the Verticillium effector
RT PevD1 and regulates the subcellular localization of cryptochrome 2.";
RL J. Exp. Bot. 68:3427-3440(2017).
CC -!- FUNCTION: Effector protein (PubMed:21691787, PubMed:24080193,
CC PubMed:24337817). Elicits a hypersensitive response (HR) in tobacco
CC plants (N.tabacum) and cotton (G.hirsutum) (PubMed:21691787,
CC PubMed:24080193, PubMed:24337817). Boosts systemic acquired resistance
CC (SAR) to tobacco mosaic virus (TMV) infection in N.tabacum and to
CC V.dhaliae infection in primed cotton seedlings (PubMed:21691787,
CC PubMed:24080193, PubMed:24337817). {ECO:0000269|PubMed:21691787,
CC ECO:0000269|PubMed:24080193, ECO:0000269|PubMed:24337817}.
CC -!- SUBUNIT: Monomer (PubMed:22750869). Interacts with Arabidopsis thaliana
CC NRP (PubMed:28633330). {ECO:0000269|PubMed:22750869,
CC ECO:0000269|PubMed:28633330}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21691787}.
CC -!- DOMAIN: The N-terminal region (1-98) is sufficient for induction of SAR
CC of N.tabacum to TMV infection. The C-terminal region (99-155) is
CC sufficient for eliciting HR in N.tabacum.
CC {ECO:0000269|PubMed:24080193}.
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DR EMBL; HQ540585; ADW79419.1; -; mRNA.
DR PDB; 5XMZ; X-ray; 1.85 A; A=1-155.
DR PDBsum; 5XMZ; -.
DR AlphaFoldDB; G0Y276; -.
DR SMR; G0Y276; -.
DR HOGENOM; CLU_144932_1_0_1; -.
DR OMA; GPADEIC; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR InterPro; IPR032382; AltA1.
DR Pfam; PF16541; AltA1; 1.
DR PROSITE; PS51895; AA1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hypersensitive response elicitation; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..155
FT /note="Effector protein PevD1"
FT /id="PRO_5003411514"
FT DOMAIN 33..148
FT /note="AA1-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01243"
FT DISULFID 70..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01243,
FT ECO:0000269|PubMed:28633330, ECO:0007744|PDB:5XMZ"
FT DISULFID 125..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01243,
FT ECO:0000269|PubMed:28633330, ECO:0007744|PDB:5XMZ"
FT CONFLICT 28
FT /note="A -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..63
FT /note="SGD -> VDAS (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 33..47
FT /evidence="ECO:0007829|PDB:5XMZ"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:5XMZ"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:5XMZ"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:5XMZ"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:5XMZ"
FT STRAND 97..107
FT /evidence="ECO:0007829|PDB:5XMZ"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:5XMZ"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:5XMZ"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:5XMZ"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5XMZ"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:5XMZ"
SQ SEQUENCE 155 AA; 16230 MW; 230EA4200C0296BF CRC64;
MQFTLAAAAA LFGASALAAP ASPGSTGAPP DPNMYENIDI ADFNVRKGED GTIKYVNFKL
SGDDADGLLC EAQNPGLPSN VITCGESKYR FALSSGKQYE FALSLYHELG LAVGFYGTGE
IFTHCRAGGL GDFICQQQNP TTIVIDSLPD APAEA
